描述：
Galectin-1, gene name LGALS1 (lectin, galactosidebinding, soluble 1), is a 135 amino acid
(aa), 14 kDa, pleiotropic, non-glycosylated, monomeric or homodimeric carbohydrate binding
protein of the prototype galectin family. Galectins lack a classical signal peptide and can be
localized to the cytosolic compartments, or secreted via nonclassical pathways. Secreted
Galectin-1 has immunosuppressive and antiinflammatory properties and suppresses acute
and chronic inflammation and autoimmunity. It contributes to negative selection of developing
T cells, immunosuppression by regulatory T cells, resolution of the inflammatory response, and
inhibition of immune cell migration, inflammatory cytokine production, and mast cell
degranulation. Galectin-1 preferentially binds laminin, fibronectin, 90K/Mac2BP, CD45, CD43,
CD7, CD2, CD3, integrins α4β1, α5β1 and α4β7,
and ganglioside GM1. It is produced in a variety of tissues by cells that include endothelial
cells, connective tissue fibroblasts, thymic stromal cells, tumor cells, muscle cells, platelets,
regulatory T cells, and activated tissue macrophages, B cells, T cells and dendritic cells. Most
of this expression is cytosolic. Mouse Galectin-1 shares 88% aa sequence identity with human,
96% with rat, and 84% with equine, ovine, bovine and porcine Galectin-1. Endothelial cell
surface expression, including tumor endothelial cells, is greatly increased by cell activation.
Galectin-1 is highly expressed at the maternalfetal interface and contributes to fetal immune
privilege. Its immunosuppressive properties appear to also allow tumor cells to evade immune
detection. It selectively controls T cell survival by inducing apoptosis of activated Th1 and Th17 cells, which express Galectin1binding glycans, while promoting Th2 cell
survival where glycans are sialylated and less recognized. It also induces apoptosis of immature
thymocytes.
Galectin-1 secreted from bone marrow stromal cells aids B lymphocyte development by
contributing to preB cell integrin adhesion and receptor signaling. The dimer form of
Galectin-1 also induces neutrophil downregulation by inducing cell surface exposure of
phosphatidylserine that marks the cell for phagocytosis. Galectin-1 can also modulate
cellcell and cellmatrix interactions, and can promote either cell attachment or detachment
depending on the cell type and developmental stage.
原厂资料：
Galectin-1, gene name LGALS1 (lectin, galactosidebinding, soluble 1), is a 135 amino acid
(aa), 14 kDa, pleiotropic, non-glycosylated, monomeric or homodimeric carbohydrate binding
protein of the prototype galectin family. Galectins lack a classical signal peptide and can be
localized to the cytosolic compartments, or secreted via nonclassical pathways. Secreted
Galectin-1 has immunosuppressive and antiinflammatory properties and suppresses acute
and chronic inflammation and autoimmunity. It contributes to negative selection of developing
T cells, immunosuppression by regulatory T cells, resolution of the inflammatory response, and
inhibition of immune cell migration, inflammatory cytokine production, and mast cell
degranulation. Galectin-1 preferentially binds laminin, fibronectin, 90K/Mac2BP, CD45, CD43,
CD7, CD2, CD3, integrins α4β1, α5β1 and α4β7,
and ganglioside GM1. It is produced in a variety of tissues by cells that include endothelial
cells, connective tissue fibroblasts, thymic stromal cells, tumor cells, muscle cells, platelets,
regulatory T cells, and activated tissue macrophages, B cells, T cells and dendritic cells. Most
of this expression is cytosolic. Mouse Galectin-1 shares 88% aa sequence identity with human,
96% with rat, and 84% with equine, ovine, bovine and porcine Galectin-1. Endothelial cell
surface expression, including tumor endothelial cells, is greatly increased by cell activation.
Galectin-1 is highly expressed at the maternalfetal interface and contributes to fetal immune
privilege. Its immunosuppressive properties appear to also allow tumor cells to evade immune
detection. It selectively controls T cell survival by inducing apoptosis of activated Th1 and Th17 cells, which express Galectin1binding glycans, while promoting Th2 cell
survival where glycans are sialylated and less recognized. It also induces apoptosis of immature
thymocytes.
Galectin-1 secreted from bone marrow stromal cells aids B lymphocyte development by
contributing to preB cell integrin adhesion and receptor signaling. The dimer form of
Galectin-1 also induces neutrophil downregulation by inducing cell surface exposure of
phosphatidylserine that marks the cell for phagocytosis. Galectin-1 can also modulate
cellcell and cellmatrix interactions, and can promote either cell attachment or detachment
depending on the cell type and developmental stage.
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